ID B2CL1_MOUSE Reviewed; 233 AA. AC Q64373; O35844; Q60657; Q60658; Q61338; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 212. DE RecName: Full=Bcl-2-like protein 1; DE Short=Bcl2-L-1; DE AltName: Full=Apoptosis regulator Bcl-X; GN Name=Bcl2l1; Synonyms=Bcl2l, Bclx; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM BCL-X(L)). RC STRAIN=2A4B; TISSUE=B-cell; RA Kamesaki H., Michaud G.Y., Takatsu K., Okuma M.; RT "IL-5 inhibits anti-IgM-induced apoptosis in an immature B cell line RT through induction of bcl-Xl."; RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)), RP DEVELOPMENTAL STAGE, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RC STRAIN=C57BL/6J; TISSUE=Brain; RX PubMed=7607090; DOI=10.1242/dev.120.10.3033; RA Gonzalez-Garcia M., Perez-Ballestero R., Ding L., Duan L., Boise L.H., RA Thompson C.B., Nunez G.; RT "bcl-XL is the major bcl-x mRNA form expressed during murine development RT and its product localizes to mitochondria."; RL Development 120:3033-3042(1994). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L); BCL-X(S) AND RP BCL-X(DELTA-TM)). RC TISSUE=Pre-B cell; RX PubMed=7963517; RA Fang W., Rivard J.J., Mueller D.L., Behrens T.W.; RT "Cloning and molecular characterization of mouse bcl-x in B and T RT lymphocytes."; RL J. Immunol. 153:4388-4398(1994). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS BCL-X(L) AND BCL-X(BETA)), AND RP FUNCTION. RC STRAIN=C57BL/6 X CBA; TISSUE=Thymus; RX PubMed=9390687; DOI=10.1016/s1074-7613(00)80384-2; RA Yang X.-F., Weber G.F., Cantor H.; RT "A novel Bcl-x isoform connected to the T cell receptor regulates apoptosis RT in T cells."; RL Immunity 7:629-639(1997). RN [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9144489; RA Grillot D.A., Gonzalez-Garcia M., Ekhterae D., Duan L., Inohara N., RA Ohta S., Seldin M.F., Nunez G.; RT "Genomic organization, promoter region analysis, and chromosome RT localization of the mouse bcl-x gene."; RL J. Immunol. 158:4750-4757(1997). RN [6] RP INTERACTION WITH GIMAP3 AND GIMAP5. RX PubMed=16509771; DOI=10.1371/journal.pbio.0040103; RA Nitta T., Nasreen M., Seike T., Goji A., Ohigashi I., Miyazaki T., Ohta T., RA Kanno M., Takahama Y.; RT "IAN family critically regulates survival and development of T RT lymphocytes."; RL PLoS Biol. 4:593-605(2006). RN [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, RC Spleen, and Testis; RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [8] RP INTERACTION WITH GIMAP5 AND HSPA8. RX PubMed=21502331; DOI=10.1084/jem.20101192; RA Chen Y., Yu M., Dai X., Zogg M., Wen R., Weiler H., Wang D.; RT "Critical role for Gimap5 in the survival of mouse hematopoietic stem and RT progenitor cells."; RL J. Exp. Med. 208:923-935(2011). RN [9] RP INTERACTION WITH BCL2L11. RX PubMed=27013495; DOI=10.15252/embr.201541392; RA Weber A., Heinlein M., Dengjel J., Alber C., Singh P.K., Haecker G.; RT "The deubiquitinase Usp27x stabilizes the BH3-only protein Bim and enhances RT apoptosis."; RL EMBO Rep. 17:724-738(2016). RN [10] RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 1-196 IN COMPLEX WITH BCL2L11. RX PubMed=14499110; DOI=10.1016/s1074-7613(03)00234-6; RA Liu X., Dai S., Zhu Y., Marrack P., Kappler J.W.; RT "The structure of a Bcl-xL/Bim fragment complex: implications for Bim RT function."; RL Immunity 19:341-352(2003). CC -!- FUNCTION: Potent inhibitor of cell death. Inhibits activation of CC caspases. Appears to regulate cell death by blocking the voltage- CC dependent anion channel (VDAC) by binding to it and preventing the CC release of the caspase activator, CYC1, from the mitochondrial CC membrane. Also acts as a regulator of G2 checkpoint and progression to CC cytokinesis during mitosis. {ECO:0000269|PubMed:9390687}. CC -!- FUNCTION: Isoform Bcl-X(L) also regulates presynaptic plasticity, CC including neurotransmitter release and recovery, number of axonal CC mitochondria as well as size and number of synaptic vesicle clusters. CC During synaptic stimulation, increases ATP availability from CC mitochondria through regulation of mitochondrial membrane ATP synthase CC F(1)F(0) activity and regulates endocytic vesicle retrieval in CC hippocampal neurons through association with DMN1L and stimulation of CC its GTPase activity in synaptic vesicles (By similarity). May attenuate CC inflammation impairing NLRP1-inflammasome activation, hence CASP1 CC activation and IL1B release (By similarity). {ECO:0000250, CC ECO:0000250|UniProtKB:Q07817}. CC -!- FUNCTION: Isoform Bcl-X(S) promotes apoptosis. {ECO:0000250}. CC -!- SUBUNIT: Homodimer. Interacts with BAD. Interacts with PGAM5. Interacts CC with HEBP2. Interacts with p53/TP53 and BBC3; interaction with BBC3 CC disrupts the interaction with p53/TP53. Interacts with ATP5F1A and CC ATP5F1B; the interactions mediate the association of isoform Bcl-X(L) CC with the mitochondrial membrane ATP synthase F(1)F(0) ATP synthase (By CC similarity). Interacts with VDAC1 (By similarity). Interacts with CC BCL2L11 (via BH3) (PubMed:14499110, PubMed:27013495). Interacts with CC RNF183 (By similarity). Interacts with GIMAP3/IAN4 and GIMAP5/IAN5 CC (PubMed:16509771). Interacts with GIMAP5 and HSPA8/HSC70; the CC interaction between HSPA8 and BCL2L1 is impaired in the absence of CC GIMAP5 (PubMed:21502331). Interacts with isoform 4 of CLU; this CC interaction releases and activates BAX and promotes cell death (By CC similarity). {ECO:0000250|UniProtKB:P53563, CC ECO:0000250|UniProtKB:Q07817, ECO:0000269|PubMed:14499110, CC ECO:0000269|PubMed:16509771, ECO:0000269|PubMed:21502331, CC ECO:0000269|PubMed:27013495}. CC -!- SUBUNIT: [Isoform Bcl-X(L)]: Forms heterodimers with BAX, BAK or BCL2; CC heterodimerization with BAX does not seem to be required for anti- CC apoptotic activity (By similarity). Interacts with isoform 1 of SIVA1; CC the interaction inhibits the anti-apoptotic activity (By similarity). CC Interacts with IKZF3 (By similarity). Interacts with RTL10/BOP (By CC similarity). Interacts with DNM1L and CLTA; DNM1L and BCL2L1 isoform CC BCL-X(L) may form a complex in synaptic vesicles that also contains CC clathrin and MFF (By similarity). Interacts (via the loop between CC motifs BH4 and BH3) with NLRP1 (via LRR repeats), but not with NLRP2, CC NLRP3, NLRP4, PYCARD, nor MEFV (By similarity). Interacts with BECN1 CC (By similarity). {ECO:0000250|UniProtKB:P53563, CC ECO:0000250|UniProtKB:Q07817}. CC -!- INTERACTION: CC Q64373; P59637: E; Xeno; NbExp=2; IntAct=EBI-526361, EBI-25487741; CC Q64373-1; Q61337: Bad; NbExp=2; IntAct=EBI-526380, EBI-400328; CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane CC {ECO:0000269|PubMed:7607090}; Single-pass membrane protein CC {ECO:0000269|PubMed:7607090}. Nucleus membrane {ECO:0000250}; Single- CC pass membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. CC Cytoplasm, cytoskeleton, microtubule organizing center, centrosome CC {ECO:0000269|PubMed:7607090}. Note=Localizes to the centrosome when CC phosphorylated at Ser-49. CC -!- SUBCELLULAR LOCATION: [Isoform Bcl-X(L)]: Mitochondrion inner membrane. CC Mitochondrion outer membrane. Mitochondrion matrix {ECO:0000250}. CC Cytoplasmic vesicle, secretory vesicle, synaptic vesicle membrane CC {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=After neuronal CC stimulation, translocates from cytosol to synaptic vesicle and CC mitochondrion membrane in a calmodulin-dependent manner. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: [Isoform Bcl-X(delta-TM)]: Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=Bcl-X(L); Synonyms=Bcl-xL; CC IsoId=Q64373-1; Sequence=Displayed; CC Name=Bcl-X(S); Synonyms=Bcl-xS; CC IsoId=Q64373-2; Sequence=VSP_000517; CC Name=Bcl-X(beta); CC IsoId=Q64373-3; Sequence=VSP_000518; CC Name=Bcl-X(delta-TM); CC IsoId=Q64373-4; Sequence=VSP_000519; CC -!- TISSUE SPECIFICITY: Widely expressed, with highest levels in the brain, CC thymus, bone marrow, and kidney. Bcl-X(L) and Bcl-X(delta-TM) CC expression is enhanced in B- and T-lymphocytes that have been CC activated. {ECO:0000269|PubMed:7607090}. CC -!- DEVELOPMENTAL STAGE: Bcl-X(beta) is expressed in both embryonal and CC postnatal tissues, whereas Bcl-X(L) is predominantly found in postnatal CC tissues. {ECO:0000269|PubMed:7607090}. CC -!- DOMAIN: The BH4 motif is required for anti-apoptotic activity. The BH1 CC and BH2 motifs are required for both heterodimerization with other Bcl- CC 2 family members and for repression of cell death. CC -!- DOMAIN: The loop between motifs BH4 and BH3 is required for the CC interaction with NLRP1. {ECO:0000250|UniProtKB:Q07817}. CC -!- PTM: Proteolytically cleaved by caspases during apoptosis. The cleaved CC protein, lacking the BH4 motif, has pro-apoptotic activity. CC {ECO:0000250}. CC -!- PTM: Phosphorylated on Ser-62 by CDK1. This phosphorylation is partial CC in normal mitotic cells, but complete in G2-arrested cells upon DNA- CC damage, thus promoting subsequent apoptosis probably by triggering CC caspases-mediated proteolysis. Phosphorylated by PLK3, leading to CC regulate the G2 checkpoint and progression to cytokinesis during CC mitosis. Phosphorylation at Ser-49 appears during the S phase and G2, CC disappears rapidly in early mitosis during prometaphase, metaphase and CC early anaphase, and re-appears during telophase and cytokinesis (By CC similarity). {ECO:0000250}. CC -!- PTM: Ubiquitinated by RNF183 during prolonged ER stress, leading to CC degradation by the proteosome. {ECO:0000250|UniProtKB:Q07817}. CC -!- SIMILARITY: Belongs to the Bcl-2 family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; X83574; CAA58557.1; -; mRNA. DR EMBL; L35049; AAA51039.1; -; mRNA. DR EMBL; L35048; AAA51040.1; -; mRNA. DR EMBL; U10102; AAA82174.1; -; mRNA. DR EMBL; U10101; AAA82173.1; -; mRNA. DR EMBL; U10100; AAA82172.1; -; mRNA. DR EMBL; U51278; AAC53459.1; -; mRNA. DR EMBL; U51279; AAC53460.1; -; mRNA. DR EMBL; U78031; AAB96881.1; -; Genomic_DNA. DR EMBL; U78030; AAB96881.1; JOINED; Genomic_DNA. DR CCDS; CCDS16899.1; -. [Q64373-1] DR PIR; I49055; I49055. DR PIR; I49056; I49056. DR PIR; I49057; I49057. DR RefSeq; NP_001276645.1; NM_001289716.1. [Q64373-1] DR RefSeq; NP_001276646.1; NM_001289717.1. [Q64373-1] DR RefSeq; NP_033873.3; NM_009743.5. [Q64373-1] DR RefSeq; XP_006498672.1; XM_006498609.3. DR RefSeq; XP_006498674.1; XM_006498611.3. DR RefSeq; XP_006498675.1; XM_006498612.2. DR RefSeq; XP_011237562.1; XM_011239260.2. DR PDB; 1PQ0; X-ray; 2.20 A; A=1-196. DR PDB; 1PQ1; X-ray; 1.65 A; A=1-196. DR PDB; 2BZW; X-ray; 2.30 A; A=1-211. DR PDB; 3IHC; X-ray; 1.85 A; A=1-196. DR PDB; 3IHD; X-ray; 1.88 A; A=1-196. DR PDB; 3IHE; X-ray; 3.00 A; A=1-196. DR PDB; 3IHF; X-ray; 2.28 A; A/B/C/D=1-196. DR PDB; 3IIG; X-ray; 2.30 A; A=1-196. DR PDB; 3IIH; X-ray; 2.75 A; A=1-196. DR PDB; 3ILB; X-ray; 2.38 A; A/N=1-196. DR PDB; 3ILC; X-ray; 1.64 A; A=1-196. DR PDB; 4YJ4; X-ray; 2.10 A; A=1-196. DR PDB; 4YK9; X-ray; 1.70 A; A/F=2-196. DR PDB; 5C3G; X-ray; 2.45 A; A=1-26. DR PDB; 7WJH; X-ray; 1.70 A; A=1-42, A=85-196. DR PDB; 7Y99; X-ray; 1.90 A; A=1-196. DR PDBsum; 1PQ0; -. DR PDBsum; 1PQ1; -. DR PDBsum; 2BZW; -. DR PDBsum; 3IHC; -. DR PDBsum; 3IHD; -. DR PDBsum; 3IHE; -. DR PDBsum; 3IHF; -. DR PDBsum; 3IIG; -. DR PDBsum; 3IIH; -. DR PDBsum; 3ILB; -. DR PDBsum; 3ILC; -. DR PDBsum; 4YJ4; -. DR PDBsum; 4YK9; -. DR PDBsum; 5C3G; -. DR PDBsum; 7WJH; -. DR PDBsum; 7Y99; -. DR AlphaFoldDB; Q64373; -. DR BMRB; Q64373; -. DR SMR; Q64373; -. DR BioGRID; 198323; 26. DR ComplexPortal; CPX-2021; BAD:BCL-XL complex. [Q64373-1] DR ComplexPortal; CPX-2025; BIM:BCL-XL complex. [Q64373-1] DR ComplexPortal; CPX-2029; PUMA:BCL-XL complex. [Q64373-1] DR ComplexPortal; CPX-2037; BID:BCL-XL complex. [Q64373-1] DR ComplexPortal; CPX-299; BCL-XL complex. [Q64373-1] DR CORUM; Q64373; -. DR ELM; Q64373; -. DR IntAct; Q64373; 9. DR STRING; 10090.ENSMUSP00000105445; -. DR BindingDB; Q64373; -. DR ChEMBL; CHEMBL3309112; -. DR iPTMnet; Q64373; -. DR PhosphoSitePlus; Q64373; -. DR EPD; Q64373; -. DR MaxQB; Q64373; -. DR PaxDb; 10090-ENSMUSP00000007803; -. DR ProteomicsDB; 273510; -. [Q64373-1] DR ProteomicsDB; 273511; -. [Q64373-2] DR ProteomicsDB; 273512; -. [Q64373-3] DR ProteomicsDB; 273513; -. [Q64373-4] DR Pumba; Q64373; -. DR Antibodypedia; 3430; 2290 antibodies from 53 providers. DR DNASU; 12048; -. DR Ensembl; ENSMUST00000007803.12; ENSMUSP00000007803.6; ENSMUSG00000007659.19. [Q64373-1] DR Ensembl; ENSMUST00000109820.5; ENSMUSP00000105445.4; ENSMUSG00000007659.19. [Q64373-1] DR Ensembl; ENSMUST00000134902.2; ENSMUSP00000134614.2; ENSMUSG00000007659.19. [Q64373-3] DR Ensembl; ENSMUST00000140436.2; ENSMUSP00000134596.2; ENSMUSG00000007659.19. [Q64373-3] DR GeneID; 12048; -. DR KEGG; mmu:12048; -. DR UCSC; uc008ngi.2; mouse. [Q64373-2] DR UCSC; uc008ngj.2; mouse. [Q64373-1] DR UCSC; uc008ngn.2; mouse. [Q64373-3] DR AGR; MGI:88139; -. DR CTD; 598; -. DR MGI; MGI:88139; Bcl2l1. DR VEuPathDB; HostDB:ENSMUSG00000007659; -. DR eggNOG; KOG4728; Eukaryota. DR GeneTree; ENSGT01090000260003; -. DR InParanoid; Q64373; -. DR OMA; RIIEWMT; -. DR OrthoDB; 4028889at2759; -. DR PhylomeDB; Q64373; -. DR TreeFam; TF315834; -. DR Reactome; R-MMU-111453; BH3-only proteins associate with and inactivate anti-apoptotic BCL-2 members. DR Reactome; R-MMU-844455; The NLRP1 inflammasome. DR Reactome; R-MMU-9648002; RAS processing. DR BioGRID-ORCS; 12048; 18 hits in 80 CRISPR screens. DR ChiTaRS; Bcl2l1; mouse. DR EvolutionaryTrace; Q64373; -. DR PRO; PR:Q64373; -. DR Proteomes; UP000000589; Chromosome 2. DR RNAct; Q64373; Protein. DR Bgee; ENSMUSG00000007659; Expressed in spermatocyte and 264 other cell types or tissues. DR ExpressionAtlas; Q64373; baseline and differential. DR GO; GO:0097136; C:Bcl-2 family protein complex; ISO:ComplexPortal. DR GO; GO:0005813; C:centrosome; ISS:UniProtKB. DR GO; GO:0005737; C:cytoplasm; ISO:MGI. DR GO; GO:0005829; C:cytosol; IDA:MGI. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI. DR GO; GO:0016020; C:membrane; IDA:MGI. DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell. DR GO; GO:0031966; C:mitochondrial membrane; IDA:MGI. DR GO; GO:0005741; C:mitochondrial outer membrane; IDA:MGI. DR GO; GO:0005739; C:mitochondrion; IDA:MGI. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0098793; C:presynapse; ISO:MGI. DR GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051400; F:BH domain binding; ISO:MGI. DR GO; GO:0051434; F:BH3 domain binding; ISO:MGI. DR GO; GO:0030276; F:clathrin binding; ISO:MGI. DR GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; ISO:MGI. DR GO; GO:0051020; F:GTPase binding; ISO:MGI. DR GO; GO:0042802; F:identical protein binding; ISO:MGI. DR GO; GO:0097371; F:MDM2/MDM4 family protein binding; ISO:MGI. DR GO; GO:0046982; F:protein heterodimerization activity; IBA:GO_Central. DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central. DR GO; GO:0019901; F:protein kinase binding; ISO:MGI. DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI. DR GO; GO:0006915; P:apoptotic process; IMP:MGI. DR GO; GO:0071839; P:apoptotic process in bone marrow cell; IMP:MGI. DR GO; GO:0071312; P:cellular response to alkaloid; IDA:MGI. DR GO; GO:0071230; P:cellular response to amino acid stimulus; IMP:MGI. DR GO; GO:0071480; P:cellular response to gamma radiation; IMP:MGI. DR GO; GO:0051607; P:defense response to virus; ISO:MGI. DR GO; GO:0097048; P:dendritic cell apoptotic process; IDA:MGI. DR GO; GO:0044565; P:dendritic cell proliferation; IDA:MGI. DR GO; GO:0035234; P:ectopic germ cell programmed cell death; IMP:MGI. DR GO; GO:0050673; P:epithelial cell proliferation; IDA:MGI. DR GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IMP:MGI. DR GO; GO:0009566; P:fertilization; IGI:MGI. DR GO; GO:0007281; P:germ cell development; IMP:MGI. DR GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI. DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI. DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI. DR GO; GO:0008584; P:male gonad development; IMP:MGI. DR GO; GO:0007005; P:mitochondrion organization; IGI:MGI. DR GO; GO:2000811; P:negative regulation of anoikis; ISO:MGI. DR GO; GO:0043066; P:negative regulation of apoptotic process; IDA:MGI. DR GO; GO:2000669; P:negative regulation of dendritic cell apoptotic process; IDA:MGI. DR GO; GO:0051093; P:negative regulation of developmental process; IMP:MGI. DR GO; GO:1902236; P:negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; ISS:UniProtKB. DR GO; GO:1900118; P:negative regulation of execution phase of apoptosis; ISS:UniProtKB. DR GO; GO:1902042; P:negative regulation of extrinsic apoptotic signaling pathway via death domain receptors; ISO:MGI. DR GO; GO:2001243; P:negative regulation of intrinsic apoptotic signaling pathway; ISO:MGI. DR GO; GO:1902230; P:negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage; ISO:MGI. DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; ISO:ComplexPortal. DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IDA:MGI. DR GO; GO:1903077; P:negative regulation of protein localization to plasma membrane; ISO:MGI. DR GO; GO:0090201; P:negative regulation of release of cytochrome c from mitochondria; ISO:ComplexPortal. DR GO; GO:2000242; P:negative regulation of reproductive process; IMP:MGI. DR GO; GO:0051402; P:neuron apoptotic process; IDA:MGI. DR GO; GO:0001541; P:ovarian follicle development; IMP:MGI. DR GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI. DR GO; GO:2001171; P:positive regulation of ATP biosynthetic process; ISO:MGI. DR GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IDA:MGI. DR GO; GO:2000809; P:positive regulation of synaptic vesicle clustering; ISO:MGI. DR GO; GO:1900244; P:positive regulation of synaptic vesicle endocytosis; ISO:MGI. DR GO; GO:2000302; P:positive regulation of synaptic vesicle exocytosis; ISO:MGI. DR GO; GO:0042981; P:regulation of apoptotic process; ISO:MGI. DR GO; GO:0032465; P:regulation of cytokinesis; ISS:UniProtKB. DR GO; GO:0040008; P:regulation of growth; IMP:MGI. DR GO; GO:1900452; P:regulation of long-term synaptic depression; ISO:MGI. DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; ISO:MGI. DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; ISO:MGI. DR GO; GO:0001836; P:release of cytochrome c from mitochondria; IGI:MGI. DR GO; GO:0046898; P:response to cycloheximide; IDA:MGI. DR GO; GO:0034097; P:response to cytokine; ISO:MGI. DR GO; GO:0002931; P:response to ischemia; ISO:MGI. DR GO; GO:0009314; P:response to radiation; IMP:MGI. DR GO; GO:0009615; P:response to virus; IDA:MGI. DR GO; GO:0007283; P:spermatogenesis; IGI:MGI. DR GO; GO:0036466; P:synaptic vesicle recycling via endosome; ISO:MGI. DR CDD; cd06845; Bcl-2_like; 1. DR DisProt; DP02817; -. DR Gene3D; 1.10.437.10; Blc2-like; 1. DR IDEAL; IID50336; -. DR InterPro; IPR013279; Apop_reg_BclX. DR InterPro; IPR036834; Bcl-2-like_sf. DR InterPro; IPR046371; Bcl-2_BH1-3. DR InterPro; IPR026298; Bcl-2_fam. DR InterPro; IPR002475; Bcl2-like. DR InterPro; IPR004725; Bcl2/BclX. DR InterPro; IPR020717; Bcl2_BH1_motif_CS. DR InterPro; IPR020726; Bcl2_BH2_motif_CS. DR InterPro; IPR020728; Bcl2_BH3_motif_CS. DR InterPro; IPR003093; Bcl2_BH4. DR InterPro; IPR020731; Bcl2_BH4_motif_CS. DR NCBIfam; TIGR00865; bcl-2; 1. DR PANTHER; PTHR11256; BCL-2 RELATED; 1. DR PANTHER; PTHR11256:SF12; BCL-2-LIKE PROTEIN 1; 1. DR Pfam; PF00452; Bcl-2; 1. DR Pfam; PF02180; BH4; 1. DR PRINTS; PR01864; APOPREGBCLX. DR PRINTS; PR01862; BCL2FAMILY. DR SMART; SM00337; BCL; 1. DR SMART; SM00265; BH4; 1. DR SUPFAM; SSF56854; Bcl-2 inhibitors of programmed cell death; 1. DR PROSITE; PS50062; BCL2_FAMILY; 1. DR PROSITE; PS01080; BH1; 1. DR PROSITE; PS01258; BH2; 1. DR PROSITE; PS01259; BH3; 1. DR PROSITE; PS01260; BH4_1; 1. DR PROSITE; PS50063; BH4_2; 1. DR Genevisible; Q64373; MM. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Apoptosis; Cytoplasm; KW Cytoplasmic vesicle; Cytoskeleton; Membrane; Mitochondrion; KW Mitochondrion inner membrane; Mitochondrion outer membrane; Nucleus; KW Phosphoprotein; Reference proteome; Synapse; Transmembrane; KW Transmembrane helix; Ubl conjugation. FT CHAIN 1..233 FT /note="Bcl-2-like protein 1" FT /id="PRO_0000143063" FT TRANSMEM 210..226 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 27..73 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 4..24 FT /note="BH4" FT MOTIF 86..100 FT /note="BH3" FT MOTIF 129..148 FT /note="BH1" FT MOTIF 180..195 FT /note="BH2" FT COMPBIAS 32..46 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 49 FT /note="Phosphoserine; by PLK3" FT /evidence="ECO:0000250|UniProtKB:Q07817" FT MOD_RES 62 FT /note="Phosphoserine; by CDK1" FT /evidence="ECO:0000250|UniProtKB:Q07817" FT VAR_SEQ 126..188 FT /note="Missing (in isoform Bcl-X(S))" FT /evidence="ECO:0000305" FT /id="VSP_000517" FT VAR_SEQ 189..233 FT /note="DTFVDLYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK -> VRT FT TPLVCPPLACVSLLCEHP (in isoform Bcl-X(beta))" FT /evidence="ECO:0000305" FT /id="VSP_000518" FT VAR_SEQ 194..233 FT /note="LYGNNAAAESRKGQERFNRWFLTGMTVAGVVLLGSLFSRK -> GHDCGWCG FT SAGLTLQSEVTRH (in isoform Bcl-X(delta-TM))" FT /evidence="ECO:0000305" FT /id="VSP_000519" FT CONFLICT 207..209 FT /note="QER -> KEG (in Ref. 4; AAC53459)" FT /evidence="ECO:0000305" FT HELIX 1..20 FT /evidence="ECO:0007829|PDB:3ILC" FT HELIX 24..27 FT /evidence="ECO:0007829|PDB:4YK9" FT HELIX 83..101 FT /evidence="ECO:0007829|PDB:3ILC" FT HELIX 102..105 FT /evidence="ECO:0007829|PDB:1PQ1" FT HELIX 106..112 FT /evidence="ECO:0007829|PDB:3ILC" FT TURN 116..118 FT /evidence="ECO:0007829|PDB:1PQ1" FT HELIX 120..127 FT /evidence="ECO:0007829|PDB:3ILC" FT HELIX 128..131 FT /evidence="ECO:0007829|PDB:3ILC" FT HELIX 137..156 FT /evidence="ECO:0007829|PDB:3ILC" FT HELIX 162..177 FT /evidence="ECO:0007829|PDB:3ILC" FT HELIX 179..184 FT /evidence="ECO:0007829|PDB:3ILC" FT HELIX 187..195 FT /evidence="ECO:0007829|PDB:3ILC" SQ SEQUENCE 233 AA; 26132 MW; 24D2AC79887E072E CRC64; MSQSNRELVV DFLSYKLSQK GYSWSQFSDV EENRTEAPEE TEAERETPSA INGNPSWHLA DSPAVNGATG HSSSLDAREV IPMAAVKQAL REAGDEFELR YRRAFSDLTS QLHITPGTAY QSFEQVVNEL FRDGVNWGRI VAFFSFGGAL CVESVDKEMQ VLVSRIASWM ATYLNDHLEP WIQENGGWDT FVDLYGNNAA AESRKGQERF NRWFLTGMTV AGVVLLGSLF SRK //